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Iron sensing and signalling

Evstatiev, Rayko, Gasche, Christoph·2012·Gut

DOI 10.1136/gut.2010.214312

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Abstract

Iron deficiency is a common condition increasingly diagnosed and treated by gastroenterologists. The most common presentation of iron deficiency is anaemia; however, it is a systemic disorder affecting multiple aspects of health in various organs. Iron is an essential element, with iron-containing proteins exerting a variety of vital functions, including oxygen transport, cellular respiration, intermediary metabolism, regulation of transcription and DNA repair. Major pathways of iron utilisation and production of iron-containing proteins include iron sulphur cluster biosynthesis, haem synthesis and storage within ferritin. The main site of iron absorption is the small intestine, but most iron is recycled by the monocyte–macrophage system via phagocytosis of senescent erythrocytes. Hepcidin, the key iron-regulating peptide binds to the iron exporter ferroportin and leads to its degradation, thereby inhibiting intestinal iron absorption and cellular export. Hepcidin levels are regulated on a transcriptional level by various stimuli, including transferrin saturation, erythropoietic activity, hypoxia and inflammation. Iron deficiency evokes adaptive responses resulting in alteration of cellular metabolism, changes in gene expression, activation of signalling pathways, cell cycle regulation, differentiation and cell death. Such responses are mediated by a number of iron-sensitive signalling pathways, including the IRE/IRP system, HIF and haem signalling. This review provides a molecular perspective for the clinician and highlights important biological aspects of iron deficiency.

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Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O 2 -Regulated Prolyl Hydroxylation
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535
Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization
Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., & Kaplan, J. (2004) · Science · doi:10.1126/science.1104742 · Cited by 4,803
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735
Anemia of Chronic Disease
Weiss, G., & Goodnough, L. T. (2005) · New England Journal of Medicine · doi:10.1056/nejmra041809 · Cited by 3,800
IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
Nemeth, E., Rivera, S., Gabayan, V., Keller, C., Taudorf, S., Pedersen, B. K., & Ganz, T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420945 · Cited by 2,650
Hepcidin, a urinary antimicrobial peptide synthesized in the liver
Park, C. H., Valore, E. V., Waring, A. J., & Ganz, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008922200 · Cited by 2,168
Balancing Acts
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736
Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667
FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
Lando, D., Peet, D. J., Gorman, J. J., Whelan, D. A., Whitelaw, M. L., & Bruick, R. K. (2002) · Genes & Development · doi:10.1101/gad.991402 · Cited by 1,550
A Novel Duodenal Iron-Regulated Transporter, IREG1, Implicated in the Basolateral Transfer of Iron to the Circulation
McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80425-6 · Cited by 1,422
The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., & Andrews, N. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.003 · Cited by 1,275
A Novel Mammalian Iron-regulated Protein Involved in Intracellular Iron Metabolism
Abboud, S., & Haile, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000713200 · Cited by 1,267
Mechanisms of Cell Protection by Heme Oxygenase-1
Gozzelino, R., Jeney, V., & Soares, M. P. (2010) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.010909.105600 · Cited by 1,241
Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 ( USF2 ) knockout mice
Nicolas, G., Bennoun, M., Devaux, I., Beaumont, C., Grandchamp, B., Kahn, A., & Vaulont, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151179498 · Cited by 1,233
Regulation of ferritin genes and protein
Torti, F. M., & Torti, S. V. (2002) · Blood · doi:10.1182/blood.v99.10.3505 · Cited by 1,173
The role of iron regulatory proteins in mammalian iron homeostasis and disease
Rouault, T. A. (2006) · Nature Chemical Biology · doi:10.1038/nchembio807 · Cited by 1,055
Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
Babitt, J. L., Huang, F. W., Wrighting, D. M., Xia, Y., Sidis, Y., Samad, T. A., Campagna, J. A., Chung, R. T., Schneyer, A. L., Woolf, C. J., et al. (2006) · Nature Genetics · doi:10.1038/ng1777 · Cited by 1,026 · cited 1×
“The R-SMAD bind to the common mediator SMAD 4 and ultimately act as a transcription factor to trigger hepcidin transcription.(98) Two highly conserved BMPresponsive elements are located in the hepcidin”
Background
A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1α regulates the VEGF expression and is potentially involved in lung and vascular development
Ema, M., Taya, S., Yokotani, N., Sogawa, K., Matsuda, Y., & Fujii-Kuriyama, Y. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4273 · Cited by 1,016
Interleukin-6 induces hepcidin expression through STAT3
Wrighting, D. M., & Andrews, N. C. (2006) · Blood · doi:10.1182/blood-2006-06-027631 · Cited by 983
Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia
Lee, P. J., Jiang, B.-H., Chin, B. Y., Iyer, N. V., Alam, J., Semenza, G. L., & Choi, A. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5375 · Cited by 782
Identification of an Intestinal Heme Transporter
Shayeghi, M., Latunde-Dada, G. O., Oakhill, J. S., Laftah, A. H., Takeuchi, K., Halliday, N., Khan, Y., Warley, A., McCann, F. E., Hider, R. C., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.025 · Cited by 755
Iron-Responsive Elements: Regulatory RNA Sequences That Control mRNA Levels and Translation
Casey, J. L., Hentze, M. W., Koeller, D. M., Caughman, S. W., Rouault, T. A., Klausner, R. D., & Harford, J. B. (1988) · Science · doi:10.1126/science.2452485 · Cited by 709
An Iron Delivery Pathway Mediated by a Lipocalin
Yang, J., Goetz, D., Li, J.-Y., Wang, W., Mori, K., Setlik, D., Du, T., Erdjument-Bromage, H., Tempst, P., Strong, R., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00710-4 · Cited by 651
Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs)
Peyssonnaux, C., Zinkernagel, A. S., Schuepbach, R. A., Rankin, E., Vaulont, S., Haase, V. H., Nizet, V., & Johnson, R. S. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31370 · Cited by 639
Mitoferrin is essential for erythroid iron assimilation
Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., Ackermann, G. E., Gwynn, B., Lambert, A. J., Wingert, R. A., Traver, D., et al. (2006) · Nature · doi:10.1038/nature04512 · Cited by 624
STAT3 mediates hepatic hepcidin expression and its inflammatory stimulation
Verga Falzacappa, M. V., Vujic Spasic, M., Kessler, R., Stolte, J., Hentze, M. W., & Muckenthaler, M. U. (2007) · Blood · doi:10.1182/blood-2006-07-033969 · Cited by 567
A cytosolic iron chaperone that delivers iron to ferritin
Shi, H., Bencze, K. Z., Stemmler, T. L., & Philpott, C. C. (2008) · Science · doi:10.1126/science.1157643 · Cited by 536
HIF-2α, but not HIF-1α, promotes iron absorption in mice
Mastrogiannaki, M., Matak, P., Keith, B., Simon, M. C., Vaulont, S., & Peyssonnaux, C. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38499 · Cited by 502
L-type Ca2+ channels provide a major pathway for iron entry into cardiomyocytes in iron-overload cardiomyopathy
Oudit, G. Y., Sun, H., Trivieri, M. G., Koch, S. E., Dawood, F., Ackerley, C., Yazdanpanah, M., Wilson, G. J., Schwartz, A., Liu, P. P., et al. (2003) · Nature Medicine · doi:10.1038/nm920 · Cited by 480
Suppression of hepcidin during anemia requires erythropoietic activity
Pak, M., Lopez, M. A., Gabayan, V., Ganz, T., & Rivera, S. (2006) · Blood · doi:10.1182/blood-2006-06-028787 · Cited by 472
Serum ferritin is derived primarily from macrophages through a nonclassical secretory pathway
Cohen, L. A., Gutierrez, L., Weiss, A., Leichtmann-Bardoogo, Y., Zhang, D.-L., Crooks, D. R., Sougrat, R., Morgenstern, A., Galy, B., Hentze, M. W., et al. (2010) · Blood · doi:10.1182/blood-2009-11-253815 · Cited by 452
Control of iron homeostasis by an iron-regulated ubiquitin ligase
Vashisht, A. A., Zumbrennen, K. B., Huang, X., Powers, D. N., Durazo, A., Sun, D., Bhaskaran, N., Persson, A., Uhlen, M., Sangfelt, O., et al. (2009) · Science · doi:10.1126/science.1176333 · Cited by 429
Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1
Rolfs, A., Kvietikova, I., Gassmann, M., & Wenger, R. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.20055 · Cited by 401
A human mitochondrial ferritin encoded by an intronless gene
Levi, S., Corsi, B., Bosisio, M., Invernizzi, R., Volz, A., Sanford, D., Arosio, P., & Drysdale, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100141200 · Cited by 400
Coordinated Remodeling of Cellular Metabolism during Iron Deficiency through Targeted mRNA Degradation
Puig, S., Askeland, E., & Thiele, D. J. (2005) · Cell · doi:10.1016/j.cell.2004.11.032 · Cited by 382
Identification of a hypoxia response element in the transferrin receptor gene
Lok, C. N., & Ponka, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24147 · Cited by 380
Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis.
The Tübingen 2000 Screen Consortium, Wingert, R. A., Galloway, J. L., Barut, B., Foott, H., Fraenkel, P., Axe, J. L., Weber, G. J., Dooley, K., Davidson, A. J., et al. (2005) · Nature · doi:10.1038/nature03887 · Cited by 370
Iron regulates ferritin mRNA translation through a segment of its 5′-untranslated region.
Aziz, N., & Munro, H. N. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8478 · Cited by 368
Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing.
Goswami, T., & Andrews, N. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600197200 · Cited by 352 · cited 1×
“Conversely, when iron-transferrin is high, HFE shuttles to TfR2 instead.(107) This TfR2eHFE interaction ultimately leads to hepcidin induction.”
Background
Binding of a Cytosolic Protein to the Iron-Responsive Element of Human Ferritin Messenger RNA
Rouault, T. A., Hentze, M. W., Caughman, S. W., Harford, J. B., & Klausner, R. D. (1988) · Science · doi:10.1126/science.3413484 · Cited by 351
Interaction of the Hereditary Hemochromatosis Protein HFE with Transferrin Receptor 2 Is Required for Transferrin-Induced Hepcidin Expression
Gao, J., Chen, J., Kramer, M., Tsukamoto, H., Zhang, A.-S., & Enns, C. A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.01.010 · Cited by 326
Carbon monoxide signals via inhibition of cytochrome c oxidase and generation of mitochondrial reactive oxygen species
Zuckerbraun, B. S., Chin, B. Y., Bilban, M., d'Avila, J. D. C., Rao, J., Billiar, T. R., & Otterbein, L. E. (2007) · The FASEB Journal · doi:10.1096/fj.06-6644com · Cited by 323
Bone morphogenetic proteins 2, 4, and 9 stimulate murine hepcidin 1 expression independently of Hfe, transferrin receptor 2 (Tfr2), and IL-6
Truksa, J., Peng, H., Lee, P., & Beutler, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603124103 · Cited by 309 · cited 1×
“124 However, intact BMP/SMAD signalling is also required for the activation of hepcidin transcription by IL-6, therefore suggesting a crosstalk between the two pathways.(96) 97 100”
Background
Synthetic hepcidin causes rapid dose-dependent hypoferremia and is concentrated in ferroportin-containing organs
Rivera, S., Nemeth, E., Gabayan, V., Lopez, M. A., Farshidi, D., & Ganz, T. (2005) · Blood · doi:10.1182/blood-2005-04-1766 · Cited by 308
Iron-regulatory proteins limit hypoxia-inducible factor-2α expression in iron deficiency
Sanchez, M., Galy, B., Muckenthaler, M. U., & Hentze, M. W. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1222 · Cited by 294
Redox signaling and cancer: The role of “labile” iron
Galaris, D., Skiada, V., & Barbouti, A. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.02.038 · Cited by 284
Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency
Mukhopadhyay, C. K., Mazumder, B., & Fox, P. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000636200 · Cited by 274
A cis-acting element is necessary and sufficient for translational regulation of human ferritin expression in response to iron.
Hentze, M. W., Rouault, T. A., Caughman, S. W., Dancis, A., Harford, J. B., & Klausner, R. D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.19.6730 · Cited by 249
Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
Cooperman, S. S., Meyron-Holtz, E. G., Olivierre-Wilson, H., Ghosh, M. C., McConnell, J. P., & Rouault, T. A. (2005) · Blood · doi:10.1182/blood-2004-12-4703 · Cited by 235
Role of the hypoxia inducible factors HIF in iron metabolism
Peyssonnaux, C., Nizet, V., & Johnson, R. S. (2008) · Cell Cycle · doi:10.4161/cc.7.1.5145 · Cited by 217
Transcriptional Remodeling in Response to Iron Deprivation in Saccharomyces cerevisiae
Shakoury-Elizeh, M., Tiedeman, J., Rashford, J., Ferea, T., Demeter, J., Garcia, E., Rolfes, R., Brown, P. O., Botstein, D., & Philpott, C. C. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0642 · Cited by 204
Transcription of the Yeast Iron Regulon Does Not Respond Directly to Iron but Rather to Iron-Sulfur Cluster Biosynthesis
Chen, O. S., Crisp, R. J., Valachovic, M., Bard, M., Winge, D. R., & Kaplan, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403209200 · Cited by 202
Carbon monoxide differentially modulates STAT1 and STAT3 and inhibits apoptosis via a phosphatidylinositol 3-kinase/Akt and p38 kinase-dependent STAT3 pathway during anoxia-reoxygenation injury
Zhang, X., Shan, P., Alam, J., Fu, X.-Y., & Lee, P. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408092200 · Cited by 198
Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum
Galy, B., Ferring-Appel, D., Kaden, S., Gröne, H.-J., & Hentze, M. W. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.006 · Cited by 195
HIF-1-mediated activation of transferrin receptor gene transcription by iron chelation
Bianchi, L., Tacchini, L., & Cairo, G. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.21.4223 · Cited by 189
Dietary Iron Supplementation Enhances DSS-Induced Colitis and Associated Colorectal Carcinoma Development in Mice
Seril, D. N., Liao, J., Ho, K.-L. K., Warsi, A., Yang, C. S., & Yang, G.-Y. (2002) · Digestive Diseases and Sciences · doi:10.1023/a:1015362228659 · Cited by 183
Intracellular labile iron
Breuer, W., Shvartsman, M., & Cabantchik, Z. I. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.03.010 · Cited by 175
Effect of oral iron supplementation on oxidative stress and colonic inflammation in rats with induced colitis
Carrier, J., Aghdassi, E., Platt, I., Cullen, J., & Allard, J. P. (2001) · Alimentary Pharmacology & Therapeutics · doi:10.1046/j.1365-2036.2001.01113.x · Cited by 169
Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation
Biederbick, A., Stehling, O., Rösser, R., Niggemeyer, B., Nakai, Y., Elsässer, H.-P., & Lill, R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00112-06 · Cited by 164
Bone morphogenetic protein (BMP)-responsive elements located in the proximal and distal hepcidin promoter are critical for its response to HJV/BMP/SMAD
Casanovas, G., Mleczko-Sanecka, K., Altamura, S., Hentze, M. W., & Muckenthaler, M. U. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0447-2 · Cited by 161
Cooperation of two mRNA-Binding proteins drives metabolic adaptation to iron deficiency
Puig, S., Vergara, S. V., & Thiele, D. J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.04.010 · Cited by 135
Iron control of erythroid development by a novel aconitase-associated regulatory pathway
Bullock, G. C., Delehanty, L. L., Talbot, A.-L., Gonias, S. L., Tong, W.-H., Rouault, T. A., Dewar, B., Macdonald, J. M., Chruma, J. J., & Goldfarb, A. N. (2010) · Blood · doi:10.1182/blood-2009-10-251496 · Cited by 85

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See all 293

Authors: Evstatiev, R., & Gasche, C.
Venue: Gut
Publisher: BMJ
Published: 2011-10-19
Volume: 61
Issue: 6
Pages: 933-952
ISSN: 0017-5749 (ISSN-L)
1468-3288
DOI: 10.1136/gut.2010.214312
OpenAlex: W2140384317
Cited by: 293
References: 62
FWCI: 13.39
Type: journal article
Language: en
Open access: closed

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Iron sensing and signalling

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